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Regulation of mTORC1 by the Rag GTPases

The Rag GTPases are an evolutionarily conserved family that play a crucial role in amino acid sensing by the mammalian target of rapamycin complex 1 (mTORC1). mTORC1 is often referred to as the master regulator of cell growth. mTORC1 hyperactivation is observed in multiple diseases such as cancer, o...

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Detalles Bibliográficos
Autores principales: Lama-Sherpa, Tshering D., Jeong, Mi-Hyeon, Jewell, Jenna L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212514/
https://www.ncbi.nlm.nih.gov/pubmed/36929165
http://dx.doi.org/10.1042/BST20210038
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author Lama-Sherpa, Tshering D.
Jeong, Mi-Hyeon
Jewell, Jenna L.
author_facet Lama-Sherpa, Tshering D.
Jeong, Mi-Hyeon
Jewell, Jenna L.
author_sort Lama-Sherpa, Tshering D.
collection PubMed
description The Rag GTPases are an evolutionarily conserved family that play a crucial role in amino acid sensing by the mammalian target of rapamycin complex 1 (mTORC1). mTORC1 is often referred to as the master regulator of cell growth. mTORC1 hyperactivation is observed in multiple diseases such as cancer, obesity, metabolic disorders, and neurodegeneration. The Rag GTPases sense amino acid levels and form heterodimers, where RagA or RagB binds to RagC or RagD, to recruit mTORC1 to the lysosome where it becomes activated. Here, we review amino acid signaling to mTORC1 through the Rag GTPases.
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spelling pubmed-102125142023-05-26 Regulation of mTORC1 by the Rag GTPases Lama-Sherpa, Tshering D. Jeong, Mi-Hyeon Jewell, Jenna L. Biochem Soc Trans Review Articles The Rag GTPases are an evolutionarily conserved family that play a crucial role in amino acid sensing by the mammalian target of rapamycin complex 1 (mTORC1). mTORC1 is often referred to as the master regulator of cell growth. mTORC1 hyperactivation is observed in multiple diseases such as cancer, obesity, metabolic disorders, and neurodegeneration. The Rag GTPases sense amino acid levels and form heterodimers, where RagA or RagB binds to RagC or RagD, to recruit mTORC1 to the lysosome where it becomes activated. Here, we review amino acid signaling to mTORC1 through the Rag GTPases. Portland Press Ltd. 2023-04-26 2023-03-16 /pmc/articles/PMC10212514/ /pubmed/36929165 http://dx.doi.org/10.1042/BST20210038 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of University of Texas Southwestern Medical Center in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with Individual.
spellingShingle Review Articles
Lama-Sherpa, Tshering D.
Jeong, Mi-Hyeon
Jewell, Jenna L.
Regulation of mTORC1 by the Rag GTPases
title Regulation of mTORC1 by the Rag GTPases
title_full Regulation of mTORC1 by the Rag GTPases
title_fullStr Regulation of mTORC1 by the Rag GTPases
title_full_unstemmed Regulation of mTORC1 by the Rag GTPases
title_short Regulation of mTORC1 by the Rag GTPases
title_sort regulation of mtorc1 by the rag gtpases
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212514/
https://www.ncbi.nlm.nih.gov/pubmed/36929165
http://dx.doi.org/10.1042/BST20210038
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